Next Article in Journal
Correction: Concha, G., et al. The Insensitivity of TASK-3 K2P Channels to External Tetraethylammonium (TEA) Partially Depends on the Cap Structure. Int. J. Mol. Sci. 2018, 19, 2437
Next Article in Special Issue
miR-7 Knockdown by Peptide Nucleic Acids in the Ascidian Ciona intestinalis
Previous Article in Journal
Retinal Ganglion Cell Death as a Late Remodeling Effect of Photoreceptor Degeneration
Previous Article in Special Issue
The ZT Biopolymer: A Self-Assembling Protein Scaffold for Stem Cell Applications
Article

Hydroxyapatite Formation on Self-Assembling Peptides with Differing Secondary Structures and Their Selective Adsorption for Proteins

National Institute of Advanced Industrial Science and Technology, 2266-98, Anagahora, Shimo-Shidami, Moriyama-ku, Nagoya, Aichi 463-8560, Japan
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2019, 20(18), 4650; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20184650
Received: 19 July 2019 / Revised: 12 September 2019 / Accepted: 17 September 2019 / Published: 19 September 2019
(This article belongs to the Special Issue Designer Biopolymers: Self-Assembling Proteins and Nucleic Acids)
Self-assembling peptides have been employed as biotemplates for biomineralization, as the morphologies and sizes of the inorganic materials can be easily controlled. We synthesized two types of highly ordered self-assembling peptides with different secondary structures and investigated the effects of secondary structures on hydroxyapatite (HAp) biomineralization of peptide templates. All as-synthesized HAp-peptides have a selective protein adsorption capacity for basic protein (e.g., cytochrome c and lysozyme). Moreover, the selectivity was improved as peptide amounts increased. In particular, peptide–HAp templated on β-sheet peptides adsorbed more cytochrome c than peptide–HAp with α-helix structures, due to the greater than 2-times carboxyl group density at their surfaces. It can be expected that self-assembled peptide-templated HAp may be used as carriers for protein immobilization in biosensing and bioseparation applications and as enzyme-stabilizing agents. View Full-Text
Keywords: solid-phase peptide synthesis; hydroxyapatite; peptide; secondary structure; selective protein adsorption; biotemplate solid-phase peptide synthesis; hydroxyapatite; peptide; secondary structure; selective protein adsorption; biotemplate
Show Figures

Graphical abstract

MDPI and ACS Style

Kojima, S.; Nakamura, H.; Lee, S.; Nagata, F.; Kato, K. Hydroxyapatite Formation on Self-Assembling Peptides with Differing Secondary Structures and Their Selective Adsorption for Proteins. Int. J. Mol. Sci. 2019, 20, 4650. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20184650

AMA Style

Kojima S, Nakamura H, Lee S, Nagata F, Kato K. Hydroxyapatite Formation on Self-Assembling Peptides with Differing Secondary Structures and Their Selective Adsorption for Proteins. International Journal of Molecular Sciences. 2019; 20(18):4650. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20184650

Chicago/Turabian Style

Kojima, Suzuka, Hitomi Nakamura, Sungho Lee, Fukue Nagata, and Katsuya Kato. 2019. "Hydroxyapatite Formation on Self-Assembling Peptides with Differing Secondary Structures and Their Selective Adsorption for Proteins" International Journal of Molecular Sciences 20, no. 18: 4650. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20184650

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop